Gen-Probe hired Morgan Stanley to seek a buyer.

Shares of Gen-Probe jumped 14 percent today after Bloomberg reported that the firm has hired Morgan Stanley to seek a buyer. Among the possible bidders listed in the article are Novartis, Thermo-Fisher Scientific, Danaher, and Life Technologies. Novartis already sells Gen-Probe's Tigris blood-screening instrument to blood banks, and it has helped fund development of Gen-Probe's new automated molecular testing platform, called Panther. The firms have collaborated since 1998 on nucleic acid tests and instruments for the blood screening market.

According to Mizuho analyst Peter Lawson, around $12 billion has been spent on diagnostics-focused merger and acquisition activity over the past year. He noted that typical molecular and proprietary-focused acquisition valuations fall into the 3x-6x price/sales range.

Two months ago, Gen-Probe reported full-year 2010 revenues of $543.3 million.

At that time, it also reported a 2 percent decrease in fourth-quarter revenues, driven by an 11 percent decline in its blood screening business. Gen-Probe attributed the decrease to lower sales of the Tigris system to Novartis, while blood screening assay sales were flat compared to the prior year.

The firm is scheduled to report its first-quarter financial results after the close of the market today.

In late Thursday trade on the Nasdaq, Gen-Probe's shares were up 14 percent at $79.99.

Its market capitalization is nearly $4 billion.

Cognizant & Eagle Genomics with Pistoia Alliance to Develop a Cloud-based Platform

Cognizant, a leading provider of consulting, technology, and business process outsourcing services, and Eagle Genomics Ltd., a bioinformatics software company specializing in genomic data management and integration, has announced they are working with the Pistoia Alliance, Inc., a nonprofit, precompetitive alliance of life science companies and vendors, as one of the groups engaged to develop a conceptual cloud-based platform to facilitate access to public and proprietary sources of gene sequence data.

The Pistoia Alliance’s sequence services working group aims to define and document an externally hosted service for securely storing and mining both proprietary derived gene/sequence information and public domain gene databases. This conceptual platform developed by Cognizant and Eagle Genomics, as part of this piloting stage, will enable working group companies to securely share their bioinformatics resources among simultaneous, registered users in a secure, encrypted environment, while leveraging the flexibility, scalability, and cost-efficiencies of a cloud-based Software as a Service (SaaS) platform. The future of collaboration and externalization within the life sciences industry will increasingly utilize hosted information services, and the Pistoia Alliance expects to run future pilots to further explore this business model involving a range of participants.

“This engagement supports the Pistoia Alliance’s goal to inspire different ways of thinking in the life sciences industry and effect real change to benefit all our organizations,” said Nick Lynch, President at Pistoia Alliance. “With the combined strengths of Cognizant and Eagle Genomics and the broader Pistoia community, we will build a platform to define standards in sequence services, while overcoming the challenges of disparate data and tools.”

Cognizant and Eagle Genomics will combine the best of their consulting, domain, technology, and business process expertise to effectively deliver the business solution. While Eagle Genomics will contribute specialized bioinformatics knowledge, Cognizant will manage the development of the platform, oversee testing and security validation, and help strengthen the initiative by managing relationships with existing and potential member organizations. The platform will deploy a secure and scalable installation of Ensembl, a software system and supporting database developed jointly by the Wellcome Trust Sanger Institute and the European Bioinformatics Institute to produce and maintain automatic annotation on selected eukaryotic genomes. The platform will deliver a Plasmapper and a gene alias service as part of the initial functional services.

Design drugs that circumvent viral drug resistance - mechanism behind Tamiflu resistance

Oseltamivir (Tamiflu) is currently the frontline antiviral drug employed to fight the flu virus in infected individuals by inhibiting neuraminidase, a flu protein responsible for the release of newly synthesized virions. However, oseltamivir resistance has become a critical problem due to rapid mutation of the flu virus. Unfortunately, how mutations actually confer drug resistance is not well understood. In this study, we employ molecular dynamics (MD) and steered molecular dynamics (SMD) simulations, as well as graphics processing unit (GPU)-accelerated electrostatic mapping, to uncover the mechanism behind point mutation induced oseltamivir-resistance in both H5N1 “avian” and H1N1pdm “swine” flu N1-subtype neuraminidases. The simulations reveal an electrostatic binding funnel that plays a key role in directing oseltamivir into and out of its binding site on N1 neuraminidase. The binding pathway for oseltamivir suggests how mutations disrupt drug binding and how new drugs may circumvent the resistance mechanisms.

Oseltamivir (Tamiflu) is the main antiviral drug used to fight viral influenza outbreaks such as the recent swine flu (H1N1pdm) global pandemic and avian (H5N1) outbreak in Asia. Oseltamivir inhibits a protein on the surface of flu viruses called neuraminidase, which is responsible for releasing newly formed viruses. The rapid emergence of drug resistance in H5N1 avian flu (and recently the H1N1pdm strain) has already motivated numerous studies to understand how mutations render oseltamivir ineffective, but no focused investigation has yet elucidated the specific mechanism behind mutation-induced drug resistance. Here, large scale computer simulations are employed to study both H5N1 and H1N1pdm neuraminidase to answer the questions: how does N1-subtype neuraminidase bind oseltamivir, and how would mutations alter this process? The key finding revealed in our simulations is the discovery of oseltamivir binding to neuraminidase by a charged pathway on the protein surface. We suggest that point mutations may disrupt drug binding by interfering with this pathway. Our results explain the fundamental mechanism behind oseltamivir resistance and pave the way for the design of drugs that circumvent viral drug resistance.

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